Fleming T M, Jones C E, Piper P W, Cowan D A, Isupov M N, Littlechild J A
Departments of Chemistry and Biological Sciences, University of Exeter, Stocker Road, Exeter EX4 4QD, England.
Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):671-4. doi: 10.1107/s0907444997018076.
Recombinant Sulfolobus solfataricus glyceraldehyde-3-phosphate dehydrogenase has been purified and found to be a tetramer of 148 kDa. The enzyme shows dual cofactor specificity and uses NADP+ in preference to NAD+. The sequence has been compared with other GAPDH proteins including those from other archaeal sources. The purified protein has been crystallized from ammonium sulfate to produce crystals that diffract to 2.4 A with a space group of P43212 or P41212. A native data set has been collected to 2.4 A using synchrotron radiation and cryocooling.
重组嗜热栖热菌甘油醛-3-磷酸脱氢酶已被纯化，发现它是一种148 kDa的四聚体。该酶表现出双重辅因子特异性，优先使用NADP⁺而非NAD⁺。已将该序列与其他甘油醛-3-磷酸脱氢酶蛋白进行了比较，包括来自其他古菌来源的蛋白。纯化后的蛋白质已从硫酸铵中结晶，产生的晶体在P43212或P41212空间群中衍射至2.4 Å。使用同步辐射和低温冷却收集了分辨率为2.4 Å的天然数据集。
